| IED ID | IndEnz0002006374 |
| Enzyme Type ID | protease006374 |
| Protein Name |
Enolase EC 4.2.1.11 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase |
| Gene Name | eno Blon_1836 BLIJ_1901 |
| Organism | Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Bifidobacteriales Bifidobacteriaceae Bifidobacterium Bifidobacterium longum Bifidobacterium longum subsp. infantis Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) |
| Enzyme Sequence | MAVIESVYARQILDSRGNPTVEVYLETEDGAQGKGLVPSGASTGEAEAWERRDGDKSVYGGKGVLNAVKAVNEVIAPKVIGMDAADQRALDDLMIELDGTPNKGKLGANAILGVSLAALYASAESAGLPLYRYIGGTNGHILPVPNMNIMNGGAHADFATDIQEYMISPYGFDTYSEALRAGVEVYHTLKNVLKKEGLNTGLGDEGGFAPKMKSNEDSLKYIMDAISAAGYEPGKQIGICLDVASSEFYNKETGKYRFDGEERDSAYMLDYYENLINEYPIVSIEDPFNEEGWEDWAAITARLGDRLQFVGDDLLVTNPARLQKAIDLGAANSLLVKLNQIGSVTETLDAIELATANGYTSMVSHRSGETPDTTISDLAVAKNTRQIKTGAPARGERVAKYNRLLEIEEELGSTAQYAGYTAFKACKKYLAK |
| Enzyme Length | 432 |
| Uniprot Accession Number | B7GTK2 |
| Absorption | |
| Active Site | ACT_SITE 205; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; ACT_SITE 337; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
| Activity Regulation | ACTIVITY REGULATION: The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}. |
| Binding Site | BINDING 155; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 164; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 285; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 312; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 337; /note=Substrate; covalent; in inhibited form; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; BINDING 388; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; |
| DNA Binding | |
| EC Number | 4.2.1.11 |
| Enzyme Function | FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (6); Chain (1); Metal binding (3); Region (1) |
| Keywords | Cytoplasm;Glycolysis;Lyase;Magnesium;Metal-binding;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,623 |
| Kinetics | |
| Metal Binding | METAL 242; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; METAL 285; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318; METAL 312; /note=Magnesium; /evidence=ECO:0000255|HAMAP-Rule:MF_00318 |
| Rhea ID | RHEA:10164 |
| Cross Reference Brenda |